Background: PNGase, also known as NGLY1 (N-glycanase 1) or PNG1, is a 654 amino acid protein that localizes to the cytoplasm and contains one PAW domain and one PUB domain. Using zinc as a cofactor, PNGase deglycosylates the denatured form of cytoplasmic N-linked glycoproteins, specifically cleaving the beta-aspartyl-glucosamine residue in the target protein and assisting in proteasome-mediated degradation. PNGase is also capable of recognizing and deglycosylating misfolded proteins in the endoplasmic reticulum (ER), thereby playing a role in the elimination of misfolded glycoproteins. PNGase exists as four alternatively spliced isoforms and is functionally inhibited by Z-VAD-fmk, a caspase inhibitor that binds to PNGase and inhibits its enzymatic activity.
Description: Rabbit polyclonal to PNGase
Immunogen: KLH conjugated synthetic peptide derived from PNGase
Specificity: ·Reacts with Human, Mouse and Rat.
.·Isotype: IgG
Application: ·Western blotting: 1/100-500. Predicted Mol wt: 74 kDa;
·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;
·Immunocytochemistry/Immunofluorescence: 1/100;
·Immunoprecipitation: 1/50;
·ELISA: 1/500;
·Optimal working dilutions must be determined by the end user.
